Self-assembly of human latexin into amyloid-like oligomers.

ABSTRACT:

Background

In conformational disorders, it is not evident which amyloid aggregates affect specific molecular mechanisms or cellular pathways, which cause disease because of their quantity and mechanical features and which states in aggregate formation are pathogenic. Due to the increasing consensus that prefibrillar oligomers play a major role in conformational diseases, there is a growing interest in understanding the characteristics of metastable polypeptide associations.

Results

Here, we show that human latexin, a protein that shares the same fold with cystatin C, assembles into stable spherical amyloid-like oligomers that bind thioflavin-T and congo red similarly to common amyloid structures but do not evolve into fibrils. Latexin self-assembly correlates with the format

SUBMITTER: Pallares I 

PROVIDER: S-EPMC2212644 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature